Laboratory of Protein Mass Spectrometry (LSMP)

Group members

• Luca Signor (CEA research engineer);
• Izabel Berard (CNRS study engineer, IE);
• Sophie Goulitquer (CNRS post-doctoral fellow);
• Julien Marcoux (PhD student);
• Shahid Mehmood (PhD student).

Presentation of the LSMP

LSMP has three complementary activities: it develops MS-based methods to obtain structure information on difficult proteins (modular, membrane or in complexes) or on their interactions, in complement which classical techniques such as crystallography, NMR or electron microscopy; it applies these developments to proteins playing major roles in human health, in collaboration with several groups.

Furthermore, it is involved in the characterization platform available for PSB members and industries (mass spectrometric analyses of proteins).

LSMP belongs to both axes “Methods and instrumentation” and “Immunity and host-pathogen interactions”.

Research topics

• Method developments;
• Structural characterization of proteins;
• Studies of protein-ligand, protein-protein and protein-membrane interactions.

Key words

Mass spectrometry, proteomics, proteins, structure, interaction, inhibitors, membrane, cross-linking, H/D exchange, quality-control, Eg5 kinesin, NADPH oxydase, Alix, CHMP proteins, translocation domain of diphtheria toxin, ADP/ATP transporter, BmrA ABC transporter.

Specialized techniques

• Mass spectrometry (ESI and MALDI)
• Protein chemistry (H/D exchange, chemical cross-linking, proteolysis)
• Liquid chromatography.

Available services

• Precise mass measurements of proteins and peptides (analysis request)
• Peptide mappings
• Locations of post-translational modifications

Major publications

Cravello L, Lascoux D & Forest E (2003). Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins. Rapid Commun Mass Spectrom 17, 2387-93 (abstract).

Loiseau L, Ollagnier-de Choudens S, Lascoux D, Forest E, Fontecave M and Barras F (2005). Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli. J Biol Chem 280, 26760-26769 (abstract).

Brier S, Lemaire D, Debonis S, Forest E & Kozielski F (2006). Molecular dissection of the inhibitor binding pocket of mitotic kinesin Eg5 reveals mutants that confer resistance to antimitotic agents J Mol Biol 360, 360-376 (abstract).

Man P, Montagner C, Vernier G., Dublet B, Chenal A, Forest E & Forge V (2007). Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry. J Mol Biol 368, 464-72 (abstract).

Lascoux D, Paramelle D, Subra G, Heymann M, Geourjon C, Martinez J & Forest E (2007). Discrimination and selective enhancement of signals in the MALDI mass spectrum of a protein by combining a matrix-based label for lysine residues with a neutral matrix. Angew Chem Int Ed 46, 5594-5597 (abstract).

Marcoux J, Man P, Castellan M, Vivès C, Forest E & Fieschi F (2009). Conformational changes in p47phox upon activation highlighted by mass spectrometry coupled to hydrogen/deuterium exchange and limited proteolysis. FEBS Lett 583, 835-840 (abstract).

(The list of all the publications of the laboratory is available here)